INTRODUCTION

Milk is a complete diet as it contains proteins ,carbohydrates, fats,

minerals, vitamins and water. The average composition of milk from different
sources is given below:

SOURCE WATE MINERAL PROTEINS FATS CARBO-HYDRATES

OF MILK R S
(%) (%) (%)
(%) (%)

Cow 87.1 0.7 3.4 3.9 4.9

Human 87.4 0.2 1.4 4.0 4.9

Goat 87 0.7 3.3 4.2 4.8

Sheep 82.6 0.9 5.5 6.5 4.5

Casein is the most predominant phosphoproteins is found in milk

an cheese. When coagulated with rennet, casein is sometimes called Paracasein.
British terminology, on the other hand, uses the term caseinogen for the
uncoagulated protein and casein for coagulated protein. As it exists in milk, it is a
salt of calcium.
Casein is not coagulated by heat. It is precipitated by acids and by
rennet enzymes, a proteolytic enzyme typically obtained from the
stomachs of calves. The enzyme trypsin can hydrolyze off a phosphate-
containing peptone.
 Casein contains a high number of proline residues, which do not interact. There are also
no disulfide bridges. As a result, it has relatively little tertiary structure. It is
relatively hydrophobic, making it poorly soluble in water. It is found in milk as a suspension of
particles, called casein micelles, which show only limited resemblance with surfactant-type
micelles in a sense that the hydrophilic parts reside at the surface and they are spherical.
However, in sharp contrast to surfactant micelles, the interior of a casein micelle is highly
hydrated. The caseins in the micelles are held together by calcium ions and hydrophobic
interactions. Any of several molecular models could account for the special conformation of
casein in the micelles. One of them proposes the micellar nucleus is formed by several
submicelles, the periphery consisting of microvellosities of κ-casein. Another model suggests
the nucleus is formed by casein-interlinked fibrils. Finally, the most recent model proposes a
double link among the caseins for gelling to take place. All three models consider micelles
as colloidal particles formed by casein aggregates wrapped up in soluble κ-casein molecules.

Ca2+ - Caesinate + 2CH3COOH(aq) Casein+(CH3COO)2Ca(aq)

The isoelectric point of casein is 4.6. Since milk's pH is 6.6, casein has a
negative charge in milk. The purified protein is water-insoluble. While it is also insoluble in
neutral salt solutions, it is readily dispersible in dilute alkalis and in salt solutions such as
aqueous sodium oxalate and sodium acetate.
 APPLICATION
In addition to being consumed in milk, casein in used in the manufacture of
adhesives, binders, protective coatings, plastics (such as for knife handles and
knitting needles), fabrics, food additives and many other products. It is commonly
used by bodybuilders as a slow-digestive source of amino acids as opposed to the
fast-digesting whey protein, and also as an extremely high source of glutamine
(post workout). Another reason it is used in bodybuilding, is because of its anti-
catabolic effect, meaning that casein consumption inhibits protein breakdown in the
body. Casein is frequently found in otherwise nondairy cheese substitutes to
improve consistency especially when melted

AIM

To study quantity of casein in different samples of milk.

Milk contains 3 to 4% casein suspended in water in the colloidal form.

It is precipitated in a weakly acidic medium.